Pub. Date : 2020 Jan 16
PMID : 31683063
2 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | We show here that both an ATP-independent protein chaperone, Spy L32P, and the FK506 binding domain of a prolyl isomerase, FKBP-25 F145A/I223P, are disordered, yet exhibit structures that are distinct from chemically denatured unfolded states in solution, and that they undergo transitions to a more structured state upon ligand binding. | Tacrolimus | FKBP prolyl isomerase 3 | Homo sapiens |
| 2 | The protein-ligand systems studied here (the ATP-independent protein chaperone, Spy L32P, and the FK506 binding domain of a prolyl isomerase, FKBP-25 F145A/I223P) may serve as models for understanding ligand-induced disorder-to-order transitions in proteins. | Tacrolimus | FKBP prolyl isomerase 3 | Homo sapiens |